A longitudinal study has been conducted on three exopeptidases which include an esterase, leucine aminopeptidase, and a triglycinopeptidase and two endopeptidases, a neutral protease and a proteinase or catheptic activity in bovine lenses. The esterase and leucine aminopeptidase behave similarily showing increased activities with aging. Triglycinopeptidase has a somewhat lower order of magnitude when compared to the other exopeptidases. The neutral protease shows initially high activity early in the developmental life period, whereas, the proteinase or catheptic activity indicates a continuous increase with aging. Data whereas, the proteinase or catheptic activity indicates a continuous increase with aging. Data is also provided on enzymic activity in the different sections of the lens which include the combined anterior cortex and epithelium, lens nucleus, posterior cortex, and equatorial ring.
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http://dx.doi.org/10.1007/BF00417288 | DOI Listing |
Bioorg Chem
December 2017
Department of Chemistry, Kurukshetra University, Kurukshetra 136119, India.
Cathepsins have emerged as promising molecular targets in a number of diseases such as Alzeimer's, inflammation and cancer. Elevated cathepsin's levels and decreased cellular inhibitor concentrations have emphasized the search for novel inhibitors of cathepsins. The present work is focused on the design and synthesis of some acetophenone phenylhydrazone based pyrazole derivatives as novel non peptidyl inhibitors of cathepsins B, H and L.
View Article and Find Full Text PDFJ Anim Sci
April 2008
Muscle Biology Group, University of Arizona, Tucson, AZ 85721, USA.
Metabolic turnover of myofibrillar proteins in skeletal muscle requires that, before being degraded to AA, myofibrillar proteins be removed from the myofibril without disrupting the ability of the myofibril to contract and develop tension. Skeletal muscle contains 4 proteolytic systems in amounts such that they could be involved in metabolic protein turnover: 1) the lysosomal system, 2) the caspase system, 3) the calpain system, and 4) the proteasome. The catheptic proteases in lysosomes are not active at the neutral pH of the cell cytoplasm, so myofibrillar proteins would have to be degraded inside lysosomes if the lysosomal system were involved.
View Article and Find Full Text PDFPhysiol Genomics
December 2006
Division of Animal and Veterinary Sciences, West Virginia University, Morgantown, WV 26506-6108, USA.
Muscle atrophy is a physiological response to diverse physiological and pathological conditions that trigger muscle deterioration through specific cellular mechanisms. Despite different signals, the biochemical changes in atrophying muscle share many common cascades. Muscle deterioration as a physiological response to the energetic demands of fish vitellogenesis represents a unique model for studying the mechanisms of muscle degradation in non-mammalian animals.
View Article and Find Full Text PDFJ Agric Food Chem
June 2004
Department of Food Science, National Taiwan Ocean University, Keelung, Taiwan 20224, Republic of China.
The recombinant and glycosylation chicken cystatins were expressed and secreted in the broth of Pichia pastoris X-33 transformant with apparent molecular masses (M) of 14 and 55 kDa, respectively. The glycosylation cystatin (glycocystatin) contained a polysaccharide chain that was composed of 50 DP of mannose residues. Because of the polymannosyl chain, the inhibitory ability in glycocystatin was 90.
View Article and Find Full Text PDFJ Biol Chem
June 2004
Department of Medicine, Washington University School of Medicine, Saint Louis, Missouri 63110, USA.
Surfactant protein D (SP-D) plays important roles in innate immunity including the defense against bacteria, fungi, and respiratory viruses. Because SP-D specifically interacts with neutrophils that infiltrate the lung in response to acute inflammation and infection, we examined the hypothesis that the neutrophil-derived serine proteinases (NSPs): neutrophil elastase, proteinase-3, and cathepsin G degrade SP-D. All three human NSPs specifically cleaved recombinant rat and natural human SP-D dodecamers in a time- and dose-dependent manner, which was reciprocally dependent on calcium concentration.
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